CADH7_ARATH
ID CADH7_ARATH Reviewed; 357 AA.
AC Q02971; B9DG76; O65622; Q53ZN3; Q9SZJ9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 7 {ECO:0000303|PubMed:14745009};
DE Short=AtCAD7 {ECO:0000303|PubMed:14745009};
DE EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
DE AltName: Full=Cinnamyl alcohol dehydrogenase-like protein B;
GN Name=CAD7; Synonyms=CAD4, CADB1, ELI3-1, LCAD-B;
GN OrderedLocusNames=At4g37980; ORFNames=F20D10.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=1464303; DOI=10.1002/j.1460-2075.1992.tb05572.x;
RA Kiedrowski S., Kawalleck P., Hahlbrock K., Somssich I.E., Dangl J.L.;
RT "Rapid activation of a novel plant defense gene is strictly dependent on
RT the Arabidopsis RPM1 disease resistance locus.";
RL EMBO J. 11:4677-4684(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14745009; DOI=10.1073/pnas.0307987100;
RA Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L.,
RA Davin L.B., Kang C., Lewis N.G.;
RT "Functional reclassification of the putative cinnamyl alcohol dehydrogenase
RT multigene family in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
RC STRAIN=cv. Columbia;
RX PubMed=10809443; DOI=10.1023/a:1006368316413;
RA Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT "Organization and structural evolution of four multigene families in
RT Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL Plant Mol. Biol. 42:703-717(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16832689; DOI=10.1007/s00425-006-0326-9;
RA Eudes A., Pollet B., Sibout R., Do C.-T., Seguin A., Lapierre C.,
RA Jouanin L.;
RT "Evidence for a role of AtCAD 1 in lignification of elongating stems of
RT Arabidopsis thaliana.";
RL Planta 225:23-39(2006).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17467016; DOI=10.1016/j.phytochem.2007.02.032;
RA Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.;
RT "Expression of cinnamyl alcohol dehydrogenases and their putative
RT homologues during Arabidopsis thaliana growth and development: lessons for
RT database annotations?";
RL Phytochemistry 68:1957-1974(2007).
CC -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step
CC specific for the production of lignin monomers. Catalyzes the NADPH-
CC dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde,
CC sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their
CC respective alcohols. {ECO:0000269|PubMed:14745009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000269|PubMed:14745009};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=320 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=3685 uM for caffeyl aldehyde (at pH 6.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=675 uM for coniferaldehyde (at pH 6.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC KM=756 uM for 5-hydroxyconiferaldehyde (at pH 6.25 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:14745009};
CC KM=373 uM for sinapaldehyde (at pH 6.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=28.6 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at
CC pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=79.0 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at
CC pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=13.0 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH
CC 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC Vmax=2.7 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as
CC substrate (at pH 6.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:14745009};
CC Vmax=0.7 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH
CC 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:14745009}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02971-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02971-2; Sequence=VSP_037892, VSP_037893;
CC -!- TISSUE SPECIFICITY: Expressed in the differentiation and elongation
CC zones of primary and lateral roots. Expressed in the hypocotyl,
CC cotyledon and leaf veins, hydathodes and trichomes. In stems, expressed
CC in the vascular cambium region. Expressed in the style, anthers, stamen
CC filaments, vascular tissues of sepals and stigmatic regions in flowers,
CC and abscission, style and stigmatic regions of siliques and seed testa.
CC {ECO:0000269|PubMed:16832689, ECO:0000269|PubMed:17467016}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X67816; CAA48027.1; -; mRNA.
DR EMBL; AY302079; AAP59432.1; -; mRNA.
DR EMBL; AL035538; CAB37538.1; -; Genomic_DNA.
DR EMBL; AL161592; CAB80463.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86859.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86860.1; -; Genomic_DNA.
DR EMBL; AF360225; AAK25935.1; -; mRNA.
DR EMBL; AY040066; AAK64124.1; -; mRNA.
DR EMBL; AY050407; AAK91423.1; -; mRNA.
DR EMBL; AY050931; AAK93608.1; -; mRNA.
DR EMBL; AY056385; AAL08241.1; -; mRNA.
DR EMBL; BT002729; AAO11645.1; -; mRNA.
DR EMBL; AK317050; BAH19743.1; -; mRNA.
DR EMBL; Y16848; CAA76419.1; -; Genomic_DNA.
DR PIR; T05625; T05625.
DR RefSeq; NP_001031805.1; NM_001036728.2. [Q02971-2]
DR RefSeq; NP_195511.1; NM_119959.4. [Q02971-1]
DR AlphaFoldDB; Q02971; -.
DR SMR; Q02971; -.
DR BioGRID; 15234; 1.
DR STRING; 3702.AT4G37980.1; -.
DR iPTMnet; Q02971; -.
DR MetOSite; Q02971; -.
DR PaxDb; Q02971; -.
DR PRIDE; Q02971; -.
DR ProteomicsDB; 223862; -. [Q02971-1]
DR EnsemblPlants; AT4G37980.1; AT4G37980.1; AT4G37980. [Q02971-1]
DR EnsemblPlants; AT4G37980.2; AT4G37980.2; AT4G37980. [Q02971-2]
DR GeneID; 829954; -.
DR Gramene; AT4G37980.1; AT4G37980.1; AT4G37980. [Q02971-1]
DR Gramene; AT4G37980.2; AT4G37980.2; AT4G37980. [Q02971-2]
DR KEGG; ath:AT4G37980; -.
DR Araport; AT4G37980; -.
DR TAIR; locus:2005527; AT4G37980.
DR eggNOG; KOG0023; Eukaryota.
DR InParanoid; Q02971; -.
DR OMA; NTGECKP; -.
DR PhylomeDB; Q02971; -.
DR BioCyc; ARA:AT4G37980-MON; -.
DR BioCyc; MetaCyc:MON-17195; -.
DR BRENDA; 1.1.1.195; 399.
DR SABIO-RK; Q02971; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q02971; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q02971; baseline and differential.
DR Genevisible; Q02971; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IGI:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lignin biosynthesis; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..357
FT /note="Cinnamyl alcohol dehydrogenase 7"
FT /id="PRO_0000160808"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 210..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 297..299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 291..298
FT /note="RKMVVGSM -> MNLFVSHL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037892"
FT VAR_SEQ 299..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037893"
FT CONFLICT 6
FT /note="E -> Q (in Ref. 1; CAA48027)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="E -> N (in Ref. 1; CAA48027)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="I -> V (in Ref. 1; CAA48027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 38246 MW; 2C27B3C2BF030166 CRC64;
MGKVLEKEAF GLAAKDESGI LSPFSFSRRA TGEKDVRFKV LFCGICHTDL SMAKNEWGLT
TYPLVPGHEI VGVVTEVGAK VKKFNAGDKV GVGYMAGSCR SCDSCNDGDE NYCPKMILTS
GAKNFDDTMT HGGYSDHMVC AEDFIIRIPD NLPLDGAAPL LCAGVTVYSP MKYHGLDKPG
MHIGVVGLGG LGHVAVKFAK AMGTKVTVIS TSERKRDEAV TRLGADAFLV SRDPKQMKDA
MGTMDGIIDT VSATHPLLPL LGLLKNKGKL VMVGAPAEPL ELPVFPLIFG RKMVVGSMVG
GIKETQEMVD LAGKHNITAD IELISADYVN TAMERLAKAD VKYRFVIDVA NTMKPTP
